shootin1 Inhibitors
Chemical inhibitors of shootin1 can exert their functional inhibitory effects through various mechanisms impacting the actin cytoskeleton and related signaling pathways, which are essential for shootin1's role in axon outgrowth and neuronal development. ML-9, for instance, targets myosin light chain kinase (MLCK), reducing the phosphorylation of myosin light chains. This action can decrease the actin-myosin interactions, vital for the cellular motility facilitated by shootin1. Similarly, Blebbistatin's inhibition of myosin II activity disrupts the rear contraction of the growth cone, a process that shootin1 supports through its interaction with actin. Cytochalasin D and Latrunculin A disrupt actin polymerization by binding to actin monomers and filaments; this can inhibit shootin1's mediation of actin dynamics, effectively inhibiting its function in cellular processes. Additionally, Y-27632's inhibition of Rho-associated protein kinase (ROCK) and NSC 23766's blockade of Rac1 activation both target pathways central to actin reorganization, thereby inhibiting processes that are dependent on shootin1's functional role.
Further, CK-666 disrupts actin filament branching by inhibiting the Arp2/3 complex, crucial for the actin dynamics within which shootin1 operates. PD 98059, by inhibiting MEK, indirectly affects the ERK signaling pathways that regulate neurite outgrowth, a process in which shootin1 is fundamentally involved. SMIFH2's disruption of formin-mediated actin assembly also directly impacts shootin1's role in axonal development. In the realm of lipid signaling, shootin1's functional role is likely impacted by Wortmannin and LY294002, both of which act as PI3K inhibitors, thus impairing the signaling pathways required for shootin1's participation in axonal guidance. Lastly, Jasplakinolide, by stabilizing actin filaments, can also inhibit the formation of new actin filaments necessary for shootin1-driven processes, demonstrating that stabilization, like depolymerization, can inhibit shootin1's activity by altering the dynamic state of actin crucial for its function.
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Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
ML-9 | 105637-50-1 | sc-200519 sc-200519A sc-200519B sc-200519C | 10 mg 50 mg 100 mg 250 mg | $112.00 $449.00 $673.00 $1224.00 | 2 | |
ML-9 is known to inhibit myosin light chain kinase (MLCK). As shootin1 is implicated in axon outgrowth and can associate with actin filaments, inhibiting MLCK can lead to decreased phosphorylation of myosin light chains, thereby reducing actin-myosin interactions and potentially inhibiting shootin1-associated axonal extension. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $72.00 $265.00 $495.00 $968.00 | ||
Blebbistatin inhibits myosin II activity. Because shootin1 is involved in the neuronal growth cone's actin dynamics, the inhibition of myosin II by Blebbistatin would likely impair the rear contraction of the growth cone mediated by shootin1's interaction with actin, leading to an inhibition of shootin1's function in cellular motility. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers and prevents their polymerization. Shootin1's function in axon outgrowth is closely linked to the regulation of actin dynamics; thus, the disruption of actin filament assembly by Latrunculin A would inhibit the cellular processes involving shootin1. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D binds to the barbed ends of actin filaments, blocking polymerization and elongation. By destabilizing actin filaments, it would inhibit the ability of shootin1 to mediate actin-driven processes like axonal outgrowth. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 is an inhibitor of Rho-associated protein kinase (ROCK). Since shootin1 has a role in growth cone dynamics and neurite outgrowth, the inhibition of ROCK, which is a downstream effector of RhoA involved in actin cytoskeleton organization, would inhibit the pathways that are crucial for shootin1's function. | ||||||
NSC 23766 | 733767-34-5 | sc-204823 sc-204823A | 10 mg 50 mg | $151.00 $609.00 | 75 | |
NSC 23766 inhibits Rac1 activation by blocking the interaction between Rac1 and its guanine nucleotide exchange factors (GEFs). Shootin1 is implicated in growth cone dynamics, which are dependent on Rac1-mediated actin reorganization, thereby inhibiting the processes that require shootin1. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
CK-666 is an inhibitor of the Arp2/3 complex, which is involved in the initiation of actin polymerization. By inhibiting the Arp2/3 complex, CK-666 would impair actin filament branching, a process that is essential for the actin dynamics where shootin1 operates in neuronal cells. | ||||||
PD 98059 | 167869-21-8 | sc-3532 sc-3532A | 1 mg 5 mg | $40.00 $92.00 | 212 | |
PD 98059 is an inhibitor of mitogen-activated protein kinase kinase (MEK), which is upstream of extracellular signal-regulated kinase (ERK) signaling. Since shootin1 is involved in the signaling pathways that regulate neurite outgrowth, the inhibition of MEK/ERK signaling would indirectly inhibit the functional role of shootin1 in these pathways. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 is a formin inhibitor, disrupting the formation of long actin filaments. Given that shootin1's functional role in axon outgrowth is linked with actin dynamics, the inhibition of formin-mediated actin assembly by SMIFH2 can inhibit shootin1's role in axonal development. | ||||||
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $67.00 $223.00 $425.00 | 97 | |
Wortmannin is a phosphoinositide 3-kinase (PI3K) inhibitor. Shootin1 associates with lipid rafts and PI3K signaling can be important for growth cone dynamics. Hence, inhibiting PI3K may impair the signaling pathways that are required for shootin1's function in axonal guidance. | ||||||